Research workbench
AlphaFold monomer V2.0 prediction for desmocollin-2 (Q02487)
Analyse AlphaFold monomer V2.0 prediction for desmocollin-2 (Q02487) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q02487
- Type
- protein
- Length
- 901 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- UniProt
- Q02487
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 901 | — | Q02487 |
Compared structures
- 5J5J · Crystal structure of a chimera of human desmocollin-2 EC1 and human desmoglein-2 EC2-EC5 · an experimental structure of the same protein · chain A against A, TM-score 0.47
- 5J5J · Crystal structure of a chimera of human Desmocollin-2 EC1 and human Desmoglein-2 EC2-EC5 · an experimental structure of the same protein · chain A against A, TM-score 0.47
- 5ERP · Crystal structure of human Desmocollin-2 ectodomain fragment EC2-5 · an experimental structure of the same protein · chain A against A, TM-score 0.45
- 5ERP · Crystal structure of human desmocollin-2 ectodomain fragment EC2-5 · an experimental structure of the same protein · chain A against A, TM-score 0.45
- 7A7D · Cadherin fit into cryo-ET map · an experimental structure of the same protein · chain A against b, TM-score 0.42
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q02487
- Elsewhere: UniProt Q02487 · AlphaFold DB Q02487
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